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7-methoxycoumarin-4-acetic acid-APGSKGDA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ASGPAGPA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DKGESGPA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DRGETGP-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DRGETGPA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DSGETGP-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-DSGETGPA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-EPGPPGPA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ERGETGPA-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ERGETGPAG-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ERGETGPAGG-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-ERGETGPSG-dinitrophenyl + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetic acid-VGPAGK-dinitrophenyl + H2O
?
-
-
-
-
?
acetyl-D-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-D-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
acetyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
acetyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-Gly-Pro-7-amino-4-trifluoromethylcoumarin
-
-
-
?
acetyl-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
acetyl-Gly-Pro + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
-
-
-
?
acetyl-Gly-Pro-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
acetyl-Gly-Pro-Gly-Pro + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
most efficient substrate, FAP shows a greater catalytic efficiency for acetyl-Gly-Pro-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate than for acetyl-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate and TSGP-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
-
?
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro-4 + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
Ala-Pro-7-amido-4-methylcoumarin + H2O
Ala-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin + H2O
-
-
-
-
?
Ala-Pro-Ala-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
Ala-Pro-Ala-Pro + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
-
-
-
?
Ala-Ser-Gly-Pro-Asn-Gln + H2O
Ala-Ser-Gly-Pro + Asn-Gln
-
-
-
?
Ala-Ser-Gly-Pro-Ser-Ser + H2O
Ala-Ser-Gly-Pro + Ser-Ser
-
-
-
?
alpha2-antiplasmin + H2O
?
alpha2-antiplasmin + H2O
truncated alpha2-antiplasmin + Met
-
-
cleaves Met from the N-terminus yielding Asn as the N-terminal amino acid
-
?
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg + H2O
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro + Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
-
-
-
-
?
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ala-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg + H2O
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ala-Pro + Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg
-
-
-
?
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ser-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg + H2O
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ser-Pro + Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg
-
-
-
?
Arg-Pro-7-amido-4-methylcoumarin + H2O
Arg-Pro + 7-amino-4-methylcoumarin
-
preferred substrate
-
-
?
B-type natriuretic peptide + H2O
?
efficiently hydrolysed and mostly preferred substrate
-
-
?
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
biotinyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
biotinyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
-
-
-
-
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
complement C1q tumor necrosis factor-related protein 6 + H2O
?
-
cleavage at position 26 after a Val-Pro sequence
-
-
?
CXCL-5 + H2O
?
-
processing of CXCL-5 at position 42, which is after an Ala-Pro sequence
-
-
?
D-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
D-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
denatured type I collagen + H2O
?
-
-
-
-
?
extracellular matrix protein 1 + H2O
?
-
cleavage occurrs at position 142 after a Lys-Pro sequence
-
-
?
extracellular matrix protein CN-I + H2O
?
-
-
-
-
?
extracellular matrix protein CN-III + H2O
?
-
-
-
-
?
extracellular matrix protein CN-V + H2O
?
-
-
-
-
?
fibrillin-2 + H2O
?
-
cleavage occurrs at position 60, in the propeptide domain, after a Gly-Pro sequence
-
-
?
GASGPAGPA + H2O
GASGP + AGPA
-
-
-
?
GEPGPPGPA + H2O
GEP + GPPGP + L-Ala
-
-
-
?
GFSPFQRED + H2O
?
low activity
-
-
?
Gln-Pro-7-amido-4-methylcoumarin + H2O
Gln-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Glu-Pro-7-amido-4-methylcoumarin + H2O
Glu-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
glucagon-like peptide-1 + H2O
?
slow hydrolysis
-
-
?
glucose-dependent insulinotropic peptide + H2O
?
slow hydrolysis
-
-
?
Gly-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin + H2O
-
-
-
?
GTAGPNQEQE + H2O
GTAGP + NQEQE
-
-
-
?
GTSGPNQEQE + H2O
GTSGP + NQEQE
-
-
-
?
Ile-Pro-7-amido-4-methylcoumarin + H2O
Ile-Pro + 7-amino-4-methylcoumarin
-
most preferred substrate
-
-
?
Ile-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ile-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
L-Ala-L-Pro-7-amido-4-methylcoumarin + H2O
L-Ala-L-Pro + 7-amino-4-methylcoumarin
-
-
-
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
L-Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Gln-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg + H2O
?
FRET-peptide
-
-
?
Leu-Pro-7-amido-4-methylcoumarin + H2O
Leu-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Ala-7-amido-4-trifluoromethylcoumarin + H2O
Lys-Ala + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Lys-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Lys-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
Lys-Pro-7-amido-4-methylcoumarin + H2O
Lys-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
lysyl oxidase homolog 2 + H2O
?
-
cleavage at position 36 after a Tyr-Pro sequence that follows the signal peptide
-
-
?
MEPLGRQLTSGP-7-amido-4-methylcoumarin + H2O
MEPLGRQLTSGP + 7-amino-4-methylcoumarin
-
-
-
?
MEPLGWQLTSGP-7-amido-4-methylcoumarin + H2O
MEPLGWQLTSGP + 7-amino-4-methylcoumarin
-
-
-
?
Met-alpha2-antiplasmin + H2O
?
Met-Pro-7-amido-4-methylcoumarin + H2O
Met-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Leu-Phe-His + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Ala + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Ala
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Glu + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Glu
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-His + H2O
N-benzyloxycarbonyl-Gly-Pro + L-His
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Leu + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Leu
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Met + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Met
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Met-His + H2O
N-benzyloxycarbonyl-Gly-Pro + Met-His
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Met-His-Arg-Ser + H2O
N-benzyloxycarbonyl-Gly-Pro + Met-His-Arg-Ser
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Phe + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Phe
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Phe-His + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Phe-L-His
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Phe-His-Arg + H2O
N-benzyloxycarbonyl-Gly-Pro + Phe-His-Arg
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Phe-His-Arg-Ser + H2O
N-benzyloxycarbonyl-Gly-Pro + Phe-His-Arg-Ser
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Ser + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Ser
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Tyr + H2O
N-benzyloxycarbonyl-Gly-Pro + L-Tyr
-
-
-
-
?
N-formyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
N-formyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
-
-
-
-
?
N-methyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin + H2O
N-methyl-Gly-Pro + 7-amino-4-methyl-3-carbamoylcoumarin
-
-
-
-
?
neuropeptide Y + H2O
?
efficiently hydrolysed and mostly preferred substrate
-
-
?
peptide YY + H2O
?
efficiently hydrolysed substrate
-
-
?
Phe-Pro-7-amido-4-methylcoumarin + H2O
Phe-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Phe-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Phe-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
pre-digested collagen + H2O
?
-
-
-
-
?
precursor Met-alpha2-antiplasmin + H2O
L-Asn-alpha2-antiplasmin + ?
-
the enzyme cleaves between Pro12 and Asn13
-
-
?
Pro-Pro-7-amido-4-methylcoumarin + H2O
Pro-Pro + 7-amino-4-methylcoumarin
-
preferred substrate
-
-
?
RPKPQQFFGLM + H2O
RPKP + L-Gln-L-Gln + FFGLM
the substance P-derived sequence is cleaved although it does not contain Gly-Pro
-
-
?
Ser-Pro-7-amido-4-methylcoumarin + H2O
Ser-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Substance P + H2O
?
efficiently hydrolysed substrate
-
-
?
Thr-Ala-Gly-Pro-Asn-Gln + H2O
Thr-Ala-Gly-Pro + Asn-Gln
-
-
-
?
Thr-Pro-7-amido-4-methylcoumarin + H2O
Thr-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Thr-Ser-Gly-Pro-Asn-Gln + H2O
Thr-Ser-Gly-Pro + Asn-Gln
-
-
-
?
Thr-Ser-Gly-Pro-Asn-Ser + H2O
Thr-Ser-Gly-Pro + Asn-Ser
-
-
-
?
Thr-Ser-Gly-Pro-Ser-Gln + H2O
Thr-Ser-Gly-Pro + Ser-Gln
-
-
-
?
Tic-Pro-7-amido-4-trifluoromethylcoumarin + H2O
?
-
-
-
-
?
TSGP-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
TSGP + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
-
-
-
?
type III collagen + H2O
?
-
-
-
-
?
type V collagen + H2O
?
-
-
-
-
?
Tyr-Pro-7-amido-4-methylcoumarin + H2O
Tyr-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Val-Pro-7-amido-4-methylcoumarin + H2O
Val-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Z-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
Ala-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
?
alpha2-antiplasmin + H2O
?
-
-
-
-
?
alpha2-antiplasmin + H2O
?
-
-
-
?
alpha2-antiplasmin + H2O
?
alpha2-antiplasmin is cleaved N-terminally to Asn-alpha2-antiplasmin that is rapidly cross-linked to fibrin and protects it from digestion by plasmin
-
-
?
alpha2-antiplasmin + H2O
?
alpha2-antiplasmin is cleaved N-terminally at Pro12-Asn13 to Asn-alpha2-antiplasmin that is rapidly cross-linked to fibrin and protects it from digestion by plasmin
-
-
?
alpha2-antiplasmin + H2O
?
efficiently hydrolysed substrate
-
-
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
cleavage of type I collagen by fibroblast activation protein-? enhances class A scavenger receptor mediated macrophage adhesion
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
seprase-dimer
-
-
?
Gelatin + H2O
?
-
gelatin cleavage results in 51 fragments
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
Met-alpha2-antiplasmin + H2O
?
-
APCE and rFAP cleave both Pro3-Leu4 and Pro12-Asn13 bonds of Met-alpha2-antiplasmin, but relative kcat /Km values for Pro12-Asn13 are about 16fold higher than for Pro3-Leu4. Conversion of Met-alpha2-antiplasmin by membrane or soluble FAP to the more easily fibrin-incorporable form, Asn-alpha2-antiplasmin, may increase plasmin inhibition within fibrin surrounding certain neoplasms and have an impact on growth and therapeutic susceptibility
-
-
?
Met-alpha2-antiplasmin + H2O
?
-
APCE and rFAP cleave both Pro3-Leu4 and Pro12-Asn13 bonds of Met-alpha2-antiplasmin, but relative kcat /Km values for Pro12-Asn13 are about 16fold higher than for Pro3-Leu4
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
additional information
?
-
-
no hydrolysis of Pro-7-amino-4-methylcoumarin, Gly-Pro-7-amino-4-methylcoumarin, Ala-Pro-7-amino-4-methylcoumarin, pGly-His-Pro-7-amino-4-methylcoumarin, N-benzyloxycarbonyl-Pro-Phe, Gly-Gly-Pro-Ala and N-benzyloxycarbonyl-Gly-Leu-Phe-His
-
-
?
additional information
?
-
glycosylated form has both postprolyl depeptidyl peptidase and postgelatinase activity, nonglycosylated isoform has no detectable gelatinase activity
-
?
additional information
?
-
-
glycosylated form has both postprolyl depeptidyl peptidase and postgelatinase activity, nonglycosylated isoform has no detectable gelatinase activity
-
?
additional information
?
-
may contribute to invasiveness in malignant cancers
-
?
additional information
?
-
-
cleaves alpha2-antiplasmin with Arg as the sixth amino acid approximately 8fold faster than alpha2-antiplasmin with Trp at this position
-
-
?
additional information
?
-
-
shows very weak activity against acetyl-Ser-Pro-7-amido-4-methylcoumarin, Asp-Pro-7-amido-4-methylcoumarin, His-Pro-7-amido-4-methylcoumarin and Asn-Pro-7-amido-4-methylcoumarin, does not cleave succinyl-Gly-Pro-7-amido-4-methyl-3-carbamoylcoumarin, Gly-Ala-7-amido-4-methylcoumarin, acetyl-Ala-Pro-7-amido-4-methylcoumarin, acetyl-Asp-Pro-7-amido-4-methylcoumarin, acetyl-Glu-Pro-7-amido-4-methylcoumarin, acetyl-Phe-Pro-7-amido-4-methylcoumarin, acetyl-His-Pro-7-amido-4-methylcoumarin, acetyl-Ile-Pro-7-amido-4-methylcoumarin, acetyl-Lys-Pro-7-amido-4-methylcoumarin, acetyl-Leu-Pro-7-amido-4-methylcoumarin, acetyl-Met-Pro-7-amido-4-methylcoumarin, acetyl-Asn-Pro-7-amido-4-methylcoumarin, acetyl-Pro-Pro-7-amido-4-methylcoumarin, acetyl-Gln-Pro-7-amido-4-methylcoumarin, acetyl-Arg-Pro-7-amido-4-methylcoumarin, acetyl-Thr-Pro-7-amido-4-methylcoumarin, acetyl-Val-Pro-7-amido-4-methylcoumarin, and acetyl-Tyr-Pro-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
FAP cleavage of peptide libraries of short amino acid sequences surrounding the scissile bond (-Pro12-Asn13-) indicates that Gly is required at position P2 and Pro is required at position P1. Arg is optimal at position P7. Peptide cleavage rate increases with Arg in position P6. Placing Arg in P4 or P8 reduces cleavage rates dramatically
-
-
?
additional information
?
-
-
FAP cleavage of peptide libraries of short amino acid sequences surrounding the scissile bond (-Pro12-Asn13-) indicates that Gly is required at position P2 and Pro is required at position P1. Arg is optimal at position P7. Peptide cleavage rate increases with Arg in position P6. Placing Arg in P4 or P8 reduces cleavage rates dramatically
-
-
?
additional information
?
-
fibroblast activation protein requires substrates with Pro at P1 and Gly or D-amino acids at P2. Besides glycine, fibroblast activation protein tolerates substrates with D-Ala and D-Ser at P2. Fibroblast activation protein prefers small, uncharged amino acids at P3, but tolerates most amino acids at P4, P1' and P2'
-
-
?
additional information
?
-
-
does not cleave native human collagens, fibronectin or laminin
-
-
?
additional information
?
-
-
FAP-alpha is an endopeptidase cleaving large protein with Gly(2)-Pro(1)-cleaving specificity
-
-
?
additional information
?
-
does not hydrolyze succinyl-L-Ala-L-Pro-7-amido-4-methylcoumarin and H-Gly-Pro-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
the enzyme acts as both a dipeptidyl peptidase and an endopeptidyl peptidase
-
-
?
additional information
?
-
a post-proline cleaving serine peptidase
-
-
?
additional information
?
-
-
a post-proline cleaving serine peptidase
-
-
?
additional information
?
-
the enzyme exhibits post-proline cleaving dipeptidyl peptidase and endopeptidase activity toward gelatin and alpha2-antiplasmin. Substrate specificity analysis using a internally quenched fluorogenic probes library for screening, overview. The sequence Pro-Tyr-Asp is strongly cleaved by the enzyme, sequence specificity, detailed overview
-
-
?
additional information
?
-
-
the enzyme exhibits post-proline cleaving dipeptidyl peptidase and endopeptidase activity toward gelatin and alpha2-antiplasmin. Substrate specificity analysis using a internally quenched fluorogenic probes library for screening, overview. The sequence Pro-Tyr-Asp is strongly cleaved by the enzyme, sequence specificity, detailed overview
-
-
?
additional information
?
-
the enzyme is a is a prolyl specific serine protease
-
-
?
additional information
?
-
-
shows no activity with Gly-Pro-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
-
?
additional information
?
-
-
the enzyme has both dipeptidyl aminopeptidase and endopeptidase activities, and can hydrolyze the post-proline bond
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-benzyl-7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
1-[(4-methoxyquinazolin-2-yl)methyl]-3,7-dimethyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-7-(3-methylbut-2-en-1-yl)-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-7-(4-methylpent-3-en-1-yl)-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
2-mercaptoethanol
inhibition at 140 mM
3,7-dimethyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
3-[[7-(but-2-yn-1-yl)-3-methyl-2,6-dioxo-8-(piperazin-1-yl)-2,3,6,7-tetrahydro-1H-purin-1-yl]methyl]benzonitrile
-
4'-[[7-(but-2-yn-1-yl)-3-methyl-2,6-dioxo-8-(piperazin-1-yl)-2,3,6,7-tetrahydro-1H-purin-1-yl]methyl]biphenyl-2-carbonitrile
-
4-(2-aminoethyl)-benzenesulfonyl fluoride hydrochloride
AEBSF, inhibition at 5 mM
4-(2-aminoethyl)-benzenesulfonylfluoride
4-amidino phenylsulfonyl fluoride
APSF, inhibition at 0.05 mM
4-amidino-phenylsulfonylfluoride
7-(but-2-yn-1-yl)-1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-1-[[2-(hydroxymethyl)-1,3-thiazol-4-yl]methyl]-3-methyl-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-1-(naphthalen-2-ylmethyl)-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-8-(piperidin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-1-[(5-methyl-2-phenyl-2H-1,2,3-triazol-4-yl)methyl]-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-1-(pyridin-2-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-1-(pyridin-3-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-1-(pyridin-4-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-(quinazolin-2-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-(quinolin-2-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-[4-(1H-1,2,4-triazol-1-yl)benzyl]-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-[4-(1H-pyrazol-1-yl)benzyl]-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-8-ethoxy-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-8-[(3S)-3-(hydroxymethyl)-5-oxopiperazin-1-yl]-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
-
7-(but-2-yn-1-yl)-8-[(8aS)-hexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
-
7-benzyl-1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
-
8-[(3R)-3-aminopiperidin-1-yl]-7-(but-2-yn-1-yl)-3-methyl-1-(propan-2-yl)-3,7-dihydro-1H-purine-2,6-dione
-
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-D-Ala-L-boroPro
-
selectively inhibits antiplasmin-cleaving enzyme vs. plasma dipeptidyl peptidase IV
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-D-Asp-L-boroPro
-
-
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-Gly-L-boroPro
-
-
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-Ser-Gly-L-boroPro
-
-
acetyl-Arg-Gly-Gly-L-boroPro
-
-
acetyl-Arg-peg-D-Asp-L-boroPro
-
-
acetyl-Arg-peg-Gly-L-boroPro
-
-
acetyl-Arg-peg-Ser-Gly-L-boroPro
-
-
acetyl-Gly-Pro-boronic acid
-
-
chymostatin
50% inhibition at 0.16 mM
diisopropyl fluorophosphate
0.005 mM
diisopropylfluorophosphate
dimethyl sulfoxide
50% inhibition at 4%
dithiothreitol
inhibition at 10 mM
FRQLTSG-pipecolinyl-NQEQV
-
L-Val-aminoacyl-proline boronic acid
PT-100
N-[(3R)-1-[7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]piperidin-3-yl]acetamide
-
N-[2-(2-cyano-4,4-difluoropyrrolidin-1-yl)-2-oxoethyl]quinoline-4-carboxamide
-
N-[2-([7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]amino)ethyl]acetamide
-
N-[2-([7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]amino)ethyl]pyridine-4-carboxamide
-
N-[2-[(2R)-2-(dihydroxyboranyl)pyrrolidin-1-yl]-2-oxoethyl]-9-N-methyl-5-oxoprolinamide
-
N2-[7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]glycinamide
-
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-(R)-fluoropyrrolidide
-
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-(S)-fluoropyrrolidide
-
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-pipecolinyl-NQEQV
-
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-piperidide
-
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-pyrrolidide
-
Phe-Gly-8-amino-3,6-dioxaoctanoyl-Gly-pipecolinyl-NQEQV
-
Phe-Gly-8-amino-3,6-dioxaoctanoyl-Gly-pipecolinyl-NQGQV
-
Phe-Gly-8-amino-3,6-dioxaoctanoyl-Gly-pyrrolidide
-
phenylmethylsulfonyl fluoride
Phenylmethylsulfonylfluoride
ValboroPro
complete inhibition at 0.05 mM
[(2R)-1-(4-oxo-4-phenylbutanoyl)pyrrolidin-2-yl]boronic acid
-
[(2R)-1-(N-acetyl-L-alanyl)pyrrolidin-2-yl]boronic acid
-
[(2R)-1-(N-acetyl-N-methylglycyl)pyrrolidin-2-yl]boronic acid
-
[(2R)-1-(N-acetylglycyl)pyrrolidin-2-yl]boronic acid
-
[(2R)-1-[(1-oxo-1,3-dihydro-2H-isoindol-2-yl)acetyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[(2-oxopyridin-1(2H)-yl)acetyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-(2,2-dimethylpropanoyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-(2-methylpropanoyl)glycyl]pyrrolidin-2-yl-9]-boronic acid
-
[(2R)-1-[N-(cyclohexylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-(cyclopentylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-(methylsulfonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-(phenylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-methyl-N-(2-methylpropanoyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-methyl-N-(phenylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
-
[(2R)-1-[N-[(2,5-dichlorophenyl)carbonyl]glycyl]-9-pyrrolidin-2-yl]boronic acid
-
[(2R)-1-[N-[(2,6-dichlorophenyl)carbonyl]glycyl]-9-pyrrolidin-2-yl]boronic acid
-
[(2S)-1-(D-valyl)pyrrolidin-2-yl]boronic acid
-
4-(2-aminoethyl)-benzenesulfonylfluoride
5 mM
4-(2-aminoethyl)-benzenesulfonylfluoride
5 mM
4-amidino-phenylsulfonylfluoride
0.5 mM
4-amidino-phenylsulfonylfluoride
0.5 mM
diisopropylfluorophosphate
-
irreversible inhibition
diisopropylfluorophosphate
inhibition at 0.005 mM
diisopropylfluorophosphate
-
50% inhibition at 0.02 mM
diisopropylfluorophosphate
0.005 mM
HgCl2
-
N-ethylmaleimide
-
phenylmethylsulfonyl fluoride
-
phenylmethylsulfonyl fluoride
-
50% inhibition at 0.1 mM
phenylmethylsulfonyl fluoride
more than 50% inhibition at 1 mM
Phenylmethylsulfonylfluoride
1 mM
Phenylmethylsulfonylfluoride
1 mM
Talabostat
-
additional information
-
not inhibited by JTP-4819, Fmoc-Ala-pyrrCN and N-benzyloxycarbonyl-Phe-Pro-BT
-
additional information
no inhibition by Z-Pro-prolinal
-
additional information
-
no inhibition by Z-Pro-prolinal
-
additional information
synthesis and inhibitory potencies of selective enzyme inhibitors from a xanthine scaffold, structure-activity relationship analysis using the crystal structures of enzyme complxed with inhibitors, overview
-
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0.051
7-methoxycoumarin-4-acetic acid-APGSKGDA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0361
7-methoxycoumarin-4-acetic acid-ASGPAGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.046
7-methoxycoumarin-4-acetic acid-DKGESGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0238
7-methoxycoumarin-4-acetic acid-DRGETGP-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.021
7-methoxycoumarin-4-acetic acid-DRGETGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0396
7-methoxycoumarin-4-acetic acid-DSGETGP-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0202
7-methoxycoumarin-4-acetic acid-DSGETGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0269
7-methoxycoumarin-4-acetic acid-EPGPPGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0567
7-methoxycoumarin-4-acetic acid-ERGETGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.043
7-methoxycoumarin-4-acetic acid-ERGETGPAG-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0371
7-methoxycoumarin-4-acetic acid-ERGETGPAGG-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.0513
7-methoxycoumarin-4-acetic acid-ERGETGPSG-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.052
7-methoxycoumarin-4-acetic acid-VGPAGK-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.541
acetyl-D-Ala-Pro-7-amido-4-trifluoromethylcoumarin
23°C
0.087 - 2.3
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
0.2 - 0.46
Ala-Pro-4-trifluoromethylcoumarin-7-amide
0.244 - 0.323
Ala-Pro-7-amido-4-trifluoromethylcoumarin
0.0022
Ala-Ser-Gly-Pro-Asn-Gln
23°C
0.0043
Ala-Ser-Gly-Pro-Ser-Ser
23°C
0.026 - 0.029
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
0.0008
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ala-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg
23°C
0.0006
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ser-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg
23°C
0.09 - 0.124
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
0.213
D-Ala-Pro-7-amido-4-trifluoromethylcoumarin
23°C
0.455 - 1
Gly-Pro-7-amido-4-methylcoumarin
0.062 - 1.8
Gly-Pro-7-amido-4-trifluoromethylcoumarin
0.106
Ile-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.2 - 0.323
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin
0.029
L-Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Gln-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
recombinant enzyme
0.189
Lys-Ala-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.9
Lys-Pro-4-trifluoromethylcoumarin-7-amide
-
pH 7.8, 37°C
0.021
MEPLGRQLTSGP-7-amido-4-methylcoumarin
pH 7.5, 22°C
0.07
MEPLGWQLTSGP-7-amido-4-methylcoumarin
pH 7.5, 22°C
0.245
Phe-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.0007
Thr-Ala-Gly-Pro-Asn-Gln
23°C
0.0013
Thr-Ser-Gly-Pro-Asn-Gln
23°C
0.0022
Thr-Ser-Gly-Pro-Asn-Ser
23°C
0.0019
Thr-Ser-Gly-Pro-Ser-Gln
23°C
0.053
Tic-Pro-7-amido-4-trifluoromethylcoumarin
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.27
Z-Gly-Pro-4-methylcoumarin-7-amide
-
-
0.087
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657N, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.1
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.14
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D/E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.33
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.42
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657T, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.43
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657V, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.48
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123K, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.51
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.52
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657S, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.57
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203A/E204A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.65
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123M, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.67
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.69
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.74
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.78
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.81
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.84
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme Y656F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.3
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.3
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme N704A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.4
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203Q/E204Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
2
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657G, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
2.3
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.2
Ala-Pro-4-trifluoromethylcoumarin-7-amide
pH 8.5
0.46
Ala-Pro-4-trifluoromethylcoumarin-7-amide
-
pH 7.8, 37°C
0.244
Ala-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.272
Ala-Pro-7-amido-4-trifluoromethylcoumarin
-
pH 7.5, 22°C, recombinant FAP
0.323
Ala-Pro-7-amido-4-trifluoromethylcoumarin
-
pH 7.5, 22°C, APCE
0.026
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
-
pH 7.5, 22°C, APCE
0.029
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
-
pH 7.5, 22°C, recombinant FAP
0.09
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
pH 7.5, 22°C
0.101
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
-
pH 7.5, 22°C, recombinant FAP
0.124
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
-
pH 7.5, 22°C, APCE
0.455
Gly-Pro-7-amido-4-methylcoumarin
pH 7.5, 22°C
1
Gly-Pro-7-amido-4-methylcoumarin
Km above 1.0 mM, wild type enzyme
0.062
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.091
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.135
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657S, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.2
Gly-Pro-7-amido-4-trifluoromethylcoumarin
Km above 0.2 mM, wild type enzyme
0.248
Gly-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
0.25
Gly-Pro-7-amido-4-trifluoromethylcoumarin
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.37
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme N704A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.38
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.41
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.42
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657T, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.44
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.45
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.49
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657V, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.55
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D/E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.67
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123M, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.73
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.75
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.92
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.1
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123K, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.1
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme Y656F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.3
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657G, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.5
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203Q/E204Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.8
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.2
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin
Km above 0.2 mM, wild type enzyme
0.25
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin
recombinant enzyme
0.323
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin
recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.015
7-methoxycoumarin-4-acetic acid-APGSKGDA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.196
7-methoxycoumarin-4-acetic acid-ASGPAGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.067
7-methoxycoumarin-4-acetic acid-DKGESGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.003
7-methoxycoumarin-4-acetic acid-DRGETGP-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.081
7-methoxycoumarin-4-acetic acid-DRGETGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.003
7-methoxycoumarin-4-acetic acid-DSGETGP-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.059
7-methoxycoumarin-4-acetic acid-DSGETGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.115
7-methoxycoumarin-4-acetic acid-EPGPPGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.141
7-methoxycoumarin-4-acetic acid-ERGETGPA-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.121
7-methoxycoumarin-4-acetic acid-ERGETGPAG-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.079
7-methoxycoumarin-4-acetic acid-ERGETGPAGG-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.268
7-methoxycoumarin-4-acetic acid-ERGETGPSG-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.095
7-methoxycoumarin-4-acetic acid-VGPAGK-dinitrophenyl
-
in 100 mM NaCl, 100 mM Tris, pH 7.8, at 37°C
0.3
acetyl-D-Ala-Pro-7-amido-4-trifluoromethylcoumarin
23°C
0.05 - 14
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
2
Ala-Pro-4-trifluoromethylcoumarin-7-amide
pH 8.5
0.995 - 14.2
Ala-Pro-7-amido-4-trifluoromethylcoumarin
2.7
Ala-Ser-Gly-Pro-Asn-Gln
23°C
5.5
Ala-Ser-Gly-Pro-Ser-Ser
23°C
1.06 - 1.2
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
0.19
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ala-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg
23°C
0.22
Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-D-Ser-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)-Arg
23°C
0.51 - 36.4
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
1.5
D-Ala-Pro-7-amido-4-trifluoromethylcoumarin
23°C
29.1
Gly-Pro-7-amido-4-methylcoumarin
pH 7.5, 22°C
0.03 - 5.6
Gly-Pro-7-amido-4-trifluoromethylcoumarin
6.9
Ile-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
1.08
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin
recombinant enzyme
1.2
L-Arg-Lys-(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Gln-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
recombinant enzyme
0.01
Lys-Ala-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
70.2
MEPLGRQLTSGP-7-amido-4-methylcoumarin
pH 7.5, 22°C
55.3
MEPLGWQLTSGP-7-amido-4-methylcoumarin
pH 7.5, 22°C
1.1
Phe-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
1.5
Thr-Ala-Gly-Pro-Asn-Gln
23°C
1.6
Thr-Ser-Gly-Pro-Asn-Gln
23°C
3.1
Thr-Ser-Gly-Pro-Asn-Ser
23°C
2
Thr-Ser-Gly-Pro-Ser-Gln
23°C
1.19
Tic-Pro-7-amido-4-trifluoromethylcoumarin
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.05
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203A/E204A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.13
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.2
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.36
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.37
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.37
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme Y656F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.4
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123K, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.45
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.47
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.48
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123M, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.6
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.94
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657V, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.4
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D/E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.8
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657G, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
2
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
4.5
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657T, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
4.7
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657S, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
7.7
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
8.9
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657N, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
14
acetyl-Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.995
Ala-Pro-7-amido-4-trifluoromethylcoumarin
-
APCE
1.08
Ala-Pro-7-amido-4-trifluoromethylcoumarin
-
pH 7.5, 22°C, recombinant FAP
6.08
Ala-Pro-7-amido-4-trifluoromethylcoumarin
-
pH 7.5, 22°C, APCE
14.2
Ala-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
1.06
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
-
pH 7.5, 22°C, APCE
1.2
Arg-Lys(4-(4-dimethylaminophenylazo)benzoyl)-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu(5-[(2-aminoethyl)amino]-naphthalene-1-sulfonic acid)-Arg
-
pH 7.5, 22°C, recombinant FAP
0.51
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
-
pH 7.5, 22°C, recombinant FAP
0.54
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
-
pH 7.5, 22°C, APCE
36.4
benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin
pH 7.5, 22°C
0.03
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.09
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.09
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657V, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.12
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme N704A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.15
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme Y656F, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.19
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.19
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204Q, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.26
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.28
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.29
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657T, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.33
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.46
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme A657S, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.71
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme E203D/E204D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.2
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123K, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
1.7
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123A, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
2.1
Gly-Pro-7-amido-4-trifluoromethylcoumarin
mutant enzyme R123M, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
5.6
Gly-Pro-7-amido-4-trifluoromethylcoumarin
-
at 23°C in 50 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, pH 7.4
5.6
Gly-Pro-7-amido-4-trifluoromethylcoumarin
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0000057
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-D-Ala-L-boroPro
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.001377
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-D-Asp-L-boroPro
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.0000018
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-Gly-L-boroPro
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.0000027
acetyl-Arg-(8-amino-3,6-dioxaoctanoic acid)-Ser-Gly-L-boroPro
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.0000172
acetyl-Arg-Gly-Gly-L-boroPro
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.023
acetyl-Gly-boro-Pro
0.0000207
acetyl-Gly-L-boroPro
-
in 25 mM sodium phosphate buffer, pH 7.5, containing 1.0 mM EDTA and 2% (v/v) methanol, at 22°C
0.000023
acetyl-Gly-Pro-boronic acid
-
-
0.014
FRQLTSG-pipecolinyl-NQEQV
pH 7.5, 22°C
0.00327
Gly-ProP(OPh)2
-
in 25 mM Tris, containing 140 mM NaCl and 10 mM KCl, pH 7.9
0.006
Leu-Pro-PO(OPh)2
-
in 25 mM Tris, containing 140 mM NaCl and 10 mM KCl, pH 7.9
0.000146
N-[2-[(2R)-2-(dihydroxyboranyl)pyrrolidin-1-yl]-2-oxoethyl]-9-N-methyl-5-oxoprolinamide
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.0553
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-(R)-fluoropyrrolidide
pH 7.5, 22°C
0.0538
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-(S)-fluoropyrrolidide
pH 7.5, 22°C
0.015
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-pipecolinyl-NQEQV
pH 7.5, 22°C
0.264
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-piperidide
pH 7.5, 22°C
0.068
Phe-Arg-8-amino-3,6-dioxaoctanoyl-Gly-pyrrolidide
pH 7.5, 22°C
0.057
Phe-Gly-8-amino-3,6-dioxaoctanoyl-Gly-pipecolinyl-NQEQV
pH 7.5, 22°C
0.0145
Phe-Gly-8-amino-3,6-dioxaoctanoyl-Gly-pipecolinyl-NQGQV
pH 7.5, 22°C
0.703
Phe-Gly-8-amino-3,6-dioxaoctanoyl-Gly-pyrrolidide
pH 7.5, 22°C
0.0046
Pro-ProP(OPh)2
-
in 25 mM Tris, containing 140 mM NaCl and 10 mM KCl, pH 7.9
0.00216
Ser-ProP(OPh)2
-
in 25 mM Tris, containing 140 mM NaCl and 10 mM KCl, pH 7.9
0.00259
Tyr-ProP(OPh)2
-
in 25 mM Tris, containing 140 mM NaCl and 10 mM KCl, pH 7.9
0.00363
Val-ProP(OPh)2
-
in 25 mM Tris, containing 140 mM NaCl and 10 mM KCl, pH 7.9
0.000094
[(2R)-1-(4-oxo-4-phenylbutanoyl)pyrrolidin-2-yl]boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.00035
[(2R)-1-(N-acetyl-L-alanyl)pyrrolidin-2-yl]boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000161
[(2R)-1-(N-acetyl-N-methylglycyl)pyrrolidin-2-yl]boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000023
[(2R)-1-(N-acetylglycyl)pyrrolidin-2-yl]boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.0000075
[(2R)-1-[(1-oxo-1,3-dihydro-2H-isoindol-2-yl)acetyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.0029
[(2R)-1-[(2-oxopyridin-1(2H)-yl)acetyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000751
[(2R)-1-[N-(2,2-dimethylpropanoyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000051
[(2R)-1-[N-(2-methylpropanoyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000014
[(2R)-1-[N-(cyclohexylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.00002
[(2R)-1-[N-(cyclopentylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000246
[(2R)-1-[N-(methylsulfonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000142
[(2R)-1-[N-(phenylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000265
[(2R)-1-[N-methyl-N-(2-methylpropanoyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000191
[(2R)-1-[N-methyl-N-(phenylcarbonyl)glycyl]pyrrolidin-2-yl]-9-boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000029
[(2R)-1-[N-[(2,5-dichlorophenyl)carbonyl]glycyl]-9-pyrrolidin-2-yl]boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.000012
[(2R)-1-[N-[(2,6-dichlorophenyl)carbonyl]glycyl]-9-pyrrolidin-2-yl]boronic acid
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.4, at 23°C
0.023
acetyl-Gly-boro-Pro
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.023
acetyl-Gly-boro-Pro
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
6.8
acetyl-Gly-Pro-CN
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
6.8
acetyl-Gly-Pro-CN
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.014
Ile-boro-Pro
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.014
Ile-boro-Pro
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.84
Ile-Pro-CN
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.84
Ile-Pro-CN
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.0062
Val-boro-Pro
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.0062
Val-boro-Pro
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.034
Val-Pro-CN
mutant enzyme A657D, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
0.034
Val-Pro-CN
wild type enzyme, at 23°C in 50 mM Tris (pH 7.4), 100 mM NaCl, and 1 mM EDTA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.1
1-benzyl-7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.1
1-[(4-methoxyquinazolin-2-yl)methyl]-3,7-dimethyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.05
1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-7-(4-methylpent-3-en-1-yl)-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
3,7-dimethyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.1
3-[[7-(but-2-yn-1-yl)-3-methyl-2,6-dioxo-8-(piperazin-1-yl)-2,3,6,7-tetrahydro-1H-purin-1-yl]methyl]benzonitrile
Homo sapiens
above, pH and temperature not specified in the publication
0.1
4'-[[7-(but-2-yn-1-yl)-3-methyl-2,6-dioxo-8-(piperazin-1-yl)-2,3,6,7-tetrahydro-1H-purin-1-yl]methyl]biphenyl-2-carbonitrile
Homo sapiens
above, pH and temperature not specified in the publication
0.0058
7-(but-2-yn-1-yl)-1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0012
7-(but-2-yn-1-yl)-1-[(4-methoxyquinazolin-2-yl)methyl]-3-methyl-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-1-[[2-(hydroxymethyl)-1,3-thiazol-4-yl]methyl]-3-methyl-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.041
7-(but-2-yn-1-yl)-3-methyl-1-(naphthalen-2-ylmethyl)-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0019
7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.00074
7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.01
7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-8-(piperidin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-3-methyl-1-[(5-methyl-2-phenyl-2H-1,2,3-triazol-4-yl)methyl]-8-(piperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.0125
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-1-(pyridin-2-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-1-(pyridin-3-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-1-(pyridin-4-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-3-methyl-8-(3-oxopiperazin-1-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.0018
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-(quinazolin-2-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.0103
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-(quinolin-2-ylmethyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-[4-(1H-1,2,4-triazol-1-yl)benzyl]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.05
7-(but-2-yn-1-yl)-3-methyl-8-(piperazin-1-yl)-1-[4-(1H-pyrazol-1-yl)benzyl]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
7-(but-2-yn-1-yl)-8-ethoxy-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.0033
7-(but-2-yn-1-yl)-8-[(3S)-3-(hydroxymethyl)-5-oxopiperazin-1-yl]-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.011
7-(but-2-yn-1-yl)-8-[(8aS)-hexahydropyrrolo[1,2-a]pyrazin-2(1H)-yl]-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
8-[(3R)-3-aminopiperidin-1-yl]-7-(but-2-yn-1-yl)-3-methyl-1-(propan-2-yl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.1
alogliptin
Homo sapiens
above, pH and temperature not specified in the publication
0.00752
dutogliptin
Homo sapiens
pH and temperature not specified in the publication
0.000089 - 0.00037
linagliptin
Homo sapiens
pH and temperature not specified in the publication
0.01
N-[(3R)-1-[7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]piperidin-3-yl]acetamide
Homo sapiens
pH and temperature not specified in the publication
0.0000033
N-[2-(2-cyano-4,4-difluoropyrrolidin-1-yl)-2-oxoethyl]quinoline-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.01
N-[2-([7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]amino)ethyl]acetamide
Homo sapiens
pH and temperature not specified in the publication
0.01
N-[2-([7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]amino)ethyl]pyridine-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.1
N2-[7-(but-2-yn-1-yl)-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]glycinamide
Homo sapiens
above, pH and temperature not specified in the publication
0.091
Phe-Arg-(8-amino-3,6-dioxaoctanoic acid)-Gly-[R]-fluoropyrrolidide
Homo sapiens
cleavage of Met-alpha2-antiplasmin
0.0026
saxagliptin
Homo sapiens
pH and temperature not specified in the publication
0.1
sitagliptin
Homo sapiens
above, pH and temperature not specified in the publication
0.00004
Talabostat
Homo sapiens
-
0.073
vildagliptin
Homo sapiens
pH and temperature not specified in the publication
0.00007
[(2S)-1-(D-valyl)pyrrolidin-2-yl]boronic acid
Homo sapiens
pH and temperature not specified in the publication
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Goldstein, L.A.; Ghersi, G.; Pineiro-Sanchez, M.L.; Salamone, M.; Yeh, Y.; Flessate, D.; Chen, W.T.
Molecular cloning of seprase: a serine integral membrane protease from human melanoma
Biochim. Biophys. Acta
1361
11-19
1997
Homo sapiens (Q12884)
brenda
Rettig, W.J.; Garin-Chesa, P.; Healey, J.H.; Su, S.L.; Ozer, H.L.; Schwab, M.; Albino, A.P.; Old, L.J.
Regulation and heteromeric structure of the fibroblast activation protein in normal and transformed cells of mesenchymal and neuroectodermal origin
Cancer Res.
53
3327-3335
1993
Homo sapiens
brenda
Rettig, W.J.; Su, S.L.; Fortunato, S.R.; Scanlan, M.J.; Raj, B.K.; Garin-Chesa, P.; Healey, J.H.; Old, L.J.
Fibroblast activation protein: purification, epitope mapping and induction by growth factors
Int. J. Cancer
58
385-392
1994
Homo sapiens
brenda
Pineiro-Sanchez, M.L.; Goldstein, L.A.; Dodt, J.; Howard, L.; Yeh, Y.; Tran, H.; Argraves, W.S.; Chen, W.T.
Identification of the 170-kDa melanoma membrane-bound gelatinase (seprase) as a serine integral membrane protease
J. Biol. Chem.
272
7595-7601
1997
Homo sapiens (Q12884), Homo sapiens
brenda
Park, J.E.; Lenter, M.C.; Zimmermann, R.N.; Garin-Chesa, P.; Old, L.J.; Rettig, W.J.
Fibroblast activation protein, a dual specificity serine protease expressed in reactive human tumor stromal fibroblasts
J. Biol. Chem.
274
36505-36512
1999
Homo sapiens
brenda
Sun, S.; Albright, C.F.; Fish, B.H.; George, H.J.; Selling, B.H.; Hollis, G.F.; Wynn, R.
Expression, purification, and kinetic characterization of full-length human fibroblast activation protein
Protein Expr. Purif.
24
274-281
2002
Homo sapiens (Q12884), Homo sapiens
brenda
Iwasa, S.; Okada, K.; Chen, W.T.; Jin, X.; Yamane, T.; Ooi, A.; Mitsumata, M.
Increased expression of seprase, a membrane-type serine protease, is associated with lymph node metastasis in human colorectal cancer
Cancer Lett.
227
229-236
2005
Homo sapiens
brenda
Huang, Y.; Wang, S.; Kelly, T.
Seprase promotes rapid tumor growth and increased microvessel density in a mouse model of human breast cancer
Cancer Res.
64
2712-2716
2004
Homo sapiens
brenda
Ghersi, G.; Zhao, Q.; Salamone, M.; Yeh, Y.; Zucker, S.; Chen, W.T.
The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices
Cancer Res.
66
4652-4661
2006
Homo sapiens
brenda
Acharya, P.S.; Zukas, A.; Chandan, V.; Katzenstein, A.L.; Pure, E.
Fibroblast activation protein: a serine protease expressed at the remodeling interface in idiopathic pulmonary fibrosis
Hum. Pathol.
37
352-360
2006
Homo sapiens
brenda
Collins, P.J.; McMahon, G.; OBrien, P.; OConnor, B.
Purification, identification and characterisation of seprase from bovine serum
Int. J. Biochem. Cell Biol.
36
2320-2333
2004
Bos taurus
brenda
Aertgeerts, K.; Levin, I.; Shi, L.; Snell, G.P.; Jennings, A.; Prasad, G.S.; Zhang, Y.; Kraus, M.L.; Salakian, S.; Sridhar, V.; Wijnands, R.; Tennant, M.G.
Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha
J. Biol. Chem.
280
19441-19444
2005
Homo sapiens
brenda
Ramirez-Montagut, T.; Blachere, N.E.; Sviderskaya, E.V.; Bennett, D.C.; Rettig, W.J.; Garin-Chesa, P.; Houghton, A.N.
FAPalpha, a surface peptidase expressed during wound healing, is a tumor suppressor
Oncogene
23
5435-5446
2004
Mus musculus, Mus musculus C57BL/6
brenda
Mori, Y.; Kono, K.; Matsumoto, Y.; Fujii, H.; Yamane, T.; Mitsumata, M.; Chen, W.T.
The expression of a type II transmembrane serine protease (Seprase) in human gastric carcinoma
Oncology
67
411-419
2004
Homo sapiens
brenda
Gilmore, B.F.; Lynas, J.F.; Scott, C.J.; McGoohan, C.; Martin, L.; Walker, B.
Dipeptide proline diphenyl phosphonates are potent, irreversible inhibitors of seprase (FAPalpha)
Biochem. Biophys. Res. Commun.
346
436-446
2006
Homo sapiens
brenda
Meadows, S.A.; Edosada, C.Y.; Mayeda, M.; Tran, T.; Quan, C.; Raab, H.; Wiesmann, C.; Wolf, B.B.
Ala657 and conserved active site residues promote fibroblast activation protein endopeptidase activity via distinct mechanisms of transition state stabilization
Biochemistry
46
4598-4605
2007
Homo sapiens (Q12884)
brenda
Aggarwal, S.; Brennen, W.N.; Kole, T.P.; Schneider, E.; Topaloglu, O.; Yates, M.; Cotter, R.J.; Denmeade, S.R.
Fibroblast activation protein peptide substrates identified from human collagen I derived gelatin cleavage sites
Biochemistry
47
1076-1086
2008
Homo sapiens
brenda
O'Brien, P.; O'Connor, B.F.
Seprase: An overview of an important matrix serine protease
Biochim. Biophys. Acta
1784
1130-1145
2008
Bos taurus, Gallus gallus, Mus musculus (P97321), Homo sapiens (Q12884), Xenopus laevis (Q91651)
brenda
Lai, K.S.; Ho, N.; Cheng, J.D.; Tung, C.
Selective fluorescence probes for dipeptidyl peptidase activity-fibroblast activation protein and dipeptidyl peptidase IV
Bioconjug. Chem.
18
1246-1250
2007
Mus musculus
brenda
Tran, T.; Quan, C.; Edosada, C.Y.; Mayeda, M.; Wiesmann, C.; Sutherlin, D.; Wolf, B.B.
Synthesis and structure-activity relationship of N-acyl-Gly-, N-acyl-Sar- and N-blocked-boroPro inhibitors of FAP, DPP4, and POP
Bioorg. Med. Chem. Lett.
17
1438-1442
2007
Homo sapiens (Q12884)
brenda
Lee, K.N.; Jackson, K.W.; Christiansen, V.J.; Lee, C.S.; Chun, J.; McKee, P.A.
Antiplasmin-cleaving enzyme is a soluble form of fibroblast activation protein
Blood
107
1397-1404
2006
Homo sapiens
brenda
Christiansen, V.J.; Jackson, K.W.; Lee, K.N.; McKee, P.A.
The effect of a single nucleotide polymorphism on human alpha 2-antiplasmin activity
Blood
109
5286-5292
2007
Homo sapiens
brenda
Ge, Y.; Zhan, F.; Barlogie, B.; Epstein, J.; Shaughnessy, J.J.; Yaccoby, S.
Fibroblast activation protein (FAP) is upregulated in myelomatous bone and supports myeloma cell survival
Br. J. Haematol.
133
83-92
2006
Homo sapiens (Q12884), Homo sapiens
brenda
Edosada, C.Y.; Quan, C.; Wiesmann, C.; Tran, T.; Sutherlin, D.; Reynolds, M.; Elliott, J.M.; Raab, H.; Fairbrother, W.; Wolf, B.B.
Selective inhibition of fibroblast activation protein protease based on dipeptide substrate specificity
J. Biol. Chem.
281
7437-7444
2006
Homo sapiens
brenda
Lee, K.N.; Jackson, K.W.; Terzyan, S.; Christiansen, V.J.; McKee,P.A.
Using substrate specificity of antiplasmin-cleaving enzyme for fibroblast activation protein inhibitor design
Biochemistry
48
5149-5158
2009
Homo sapiens (Q12884), Homo sapiens
brenda
Edosada, C.Y.; Quan, C.; Tran, T.; Pham, V.; Wiesmann, C.; Fairbrother, W.; Wolf, B.B.
Peptide substrate profiling defines fibroblast activation protein as an endopeptidase of strict Gly(2)-Pro(1)-cleaving specificity
FEBS Lett.
580
1581-1586
2006
Homo sapiens (Q12884)
brenda
Kennedy, A.; Dong, H.; Chen, D.; Chen, W.T.
Elevation of seprase expression and promotion of an invasive phenotype by collagenous matrices in ovarian tumor cells
Int. J. Cancer
124
27-35
2009
Homo sapiens (Q12884)
brenda
Goscinski, M.A.; Suo, Z.H.; Nesland, J.M.; Chen, W.T.; Zakrzewska, M.; Wang, J.; Zhang, S.; Florenes, V.A.; Giercksky, K.E.
Seprase, dipeptidyl peptidase IV and urokinase-type plasminogen activator expression in dysplasia and invasive squamous cell carcinoma of the esophagus. A study of 229 cases from Anyang Tumor Hospital, Henan Province, China
Oncology
75
49-59
2008
Homo sapiens (Q12884)
brenda
Mentlein, R.; Hattermann, K.; Hemion, C.; Jungbluth, A.; Held-Feindt, J.
Expression and role of the cell surface protease seprase/fibroblast activation protein-alpha (FAP-alpha) in astroglial tumors
Biol. Chem.
392
199-207
2011
Homo sapiens
brenda
Keane, F.; Nadvi, N.; Yao, T.; Gorrell, M.
Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are novel substrates of fibroblast activation protein-alpha
FEBS J.
278
1316-1332
2011
Homo sapiens (Q12884)
brenda
Lee, K.; Jackson, K.; Christiansen, V.; Dolence, E.; Mckee, P.
Enhancement of fibrinolysis by inhibiting enzymatic cleavage of precursor alpha2-antiplasmin
J. Thromb. Haemost.
9
987-996
2011
Homo sapiens
brenda
Yang, L.; Ma, L.; Lai, D.
Over-expression of fibroblast activation protein alpha increases tumor growth in xenografts of ovarian cancer cells
Acta Biochim. Biophys. Sin. (Shanghai)
45
928-937
2013
Homo sapiens (Q12844)
brenda
Jia, J.; Martin, T.A.; Ye, L.; Jiang, W.G.
FAP-alpha (fibroblast activation protein-alpha) is involved in the control of human breast cancer cell line growth and motility via the FAK pathway
BMC Cell Biol.
15
16
2014
Homo sapiens (Q12844)
brenda
Yang, W.; Han, W.; Ye, S.; Liu, D.; Wu, J.; Liu, H.; Li, C.; Chen, H.
Fibroblast activation protein-alpha promotes ovarian cancer cell proliferation and invasion via extracellular and intracellular signaling mechanisms
Exp. Mol. Pathol.
95
105-110
2013
Homo sapiens (Q12844)
brenda
Jambunathan, K.; Watson, D.S.; Endsley, A.N.; Kodukula, K.; Galande, A.K.
Comparative analysis of the substrate preferences of two post-proline cleaving endopeptidases, prolyl oligopeptidase and fibroblast activation protein alpha
FEBS Lett.
586
2507-2512
2012
Homo sapiens (Q12844), Homo sapiens
brenda
Keane, F.M.; Yao, T.W.; Seelk, S.; Gall, M.G.; Chowdhury, S.; Poplawski, S.E.; Lai, J.H.; Li, Y.; Wu, W.; Farrell, P.; Vieira de Ribeiro, A.J.; Osborne, B.; Yu, D.M.; Seth, D.; Rahman, K.; Haber, P.; Topaloglu, A.K.; Wang, C.; Thomson, S.; Hennessy, A.; Prins, J.; Twigg, S.M.; McLennan, S.V.; McCaughan, G.W.; Ba, B.a.c.
Quantitation of fibroblast activation protein (FAP)-specific protease activity in mouse, baboon and human fluids and organs
FEBS open bio
4
43-54
2013
Papio sp., Mus musculus (P97321), Mus musculus, Homo sapiens (Q12844), Homo sapiens
brenda
Jansen, K.; De Winter, H.; Heirbaut, L.; Cheng, J.; Joossens, J.; Lambeir, A.; De Meester, I.; Augustyns, K.; Van Der Veken, P.
Selective inhibitors of fibroblast activation protein (FAP) with a xanthine scaffold
MedChemComm
5
1700-1707
2013
Homo sapiens (Q12844)
-
brenda
Knopf, J.D.; Tholen, S.; Koczorowska, M.M.; De Wever, O.; Biniossek, M.L.; Schilling, O.
The stromal cell-surface protease fibroblast activation protein-alpha localizes to lipid rafts and is recruited to invadopodia
Biochim. Biophys. Acta
1853
2515-2525
2015
Homo sapiens
brenda
Liu, J.; Huang, C.; Peng, C.; Xu, F.; Li, Y.; Yutaka, Y.; Xiong, B.; Yang, X.
Stromal fibroblast activation protein alpha promotes gastric cancer progression via epithelial-mesenchymal transition through Wnt/ beta-catenin pathway
BMC Cancer
18
1099
2018
Homo sapiens
brenda
Lv, B.; Xie, F.; Zhao, P.; Ma, X.; Jiang, W.; Yu, J.; Zhang, X.; Jia, J.
Promotion of cellular growth and motility is independent of enzymatic activity of fibroblast activation protein-alpha
Cancer Genomics Proteomics
13
201-208
2016
Homo sapiens
brenda
Bracke, A.; Van Elzen, R.; Van Der Veken, P.; Augustyns, K.; De Meester, I.; Lambeir, A.M.
The development and validation of a combined kinetic fluorometric activity assay for fibroblast activation protein alpha and prolyl oligopeptidase in plasma
Clin. Chim. Acta
495
154-160
2019
Homo sapiens
brenda
Busek, P.; Hrabal, P.; Fric, P.; Sedo, A.
Co-expression of the homologous proteases fibroblast activation protein and dipeptidyl peptidase-IV in the adult human Langerhans islets
Histochem. Cell Biol.
143
497-504
2015
Homo sapiens
-
brenda
Jia, J.; Martin, T.A.; Ye, L.; Meng, L.; Xia, N.; Jiang, W.G.; Zhang, X.
Fibroblast activation protein-alpha promotes the growth and migration of lung cancer cells via the PI3K and sonic hedgehog pathways
Int. J. Mol. Med.
41
275-283
2018
Homo sapiens
brenda
Zhang, H.E.; Hamson, E.J.; Koczorowska, M.M.; Tholen, S.; Chowdhury, S.; Bailey, C.G.; Lay, A.J.; Twigg, S.M.; Lee, Q.; Roediger, B.; Biniossek, M.L.; ORourke, M.B.; McCaughan, G.W.; Keane, F.M.; Schilling, O.; Gorrell, M.D.
Identification of novel natural substrates of fibroblast activation protein-alpha by differential degradomics and proteomics
Mol. Cell. Proteomics
18
65-85
2019
Mus musculus
brenda
Mazur, A.; Holthoff, E.; Vadali, S.; Kelly, T.; Post, S.R.
Cleavage of type I collagen by fibroblast activation protein-alpha enhances class A scavenger receptor mediated macrophage adhesion
PLoS ONE
11
e0150287
2016
Mus musculus
brenda
Gunderson, A.; Yamazaki, T.; McCarty, K.; Phillips, M.; Alice, A.; Bambina, S.; Zebertavage, L.; Friedman, D.; Cottam, B.; Newell, P.; Gough, M.; Crittenden, M.; Van der Veken, P.; Young, K.
Blockade of fibroblast activation protein in combination with radiation treatment in murine models of pancreatic adenocarcinoma
PLoS ONE
14
e0211117
2019
Homo sapiens
brenda
Busek, P.; Balaziova, E.; Matrasova, I.; Hilser, M.; Tomas, R.; Syrucek, M.; Zemanova, Z.; Krepela, E.; Belacek, J.; Sedo, A.
Fibroblast activation protein alpha is expressed by transformed and stromal cells and is associated with mesenchymal features in glioblastoma
Tumour Biol.
37
13961-13971
2016
Homo sapiens
brenda